On the functional heterogeneity of UDP-glucuronyl transferase of mouse liver microsomes.
Fractionation of sodium cholate solubilized microsomes from mouse liver on Sepharose CL-48 yielded three protein peaks with UDP-glucuronyltransferase activities. Of these three peaks, only peak II contained activities towards all the substrates tested: p-nitrophenol, 1-naphthol, morphine, testosterone and estrone. These glucuronyltransferase activities could not be dissociated by further chromatography on DEAE-Sepharose CL-6B and isoelectric focusing. The results show the presence of a functional form of glucuronyltransferase with a wide substrate specificity, and indicate that in addition, other forms with narrower studied specificities may also be present in mouse liver microsomes.
D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005260:Female; D014453:Glucuronosyltransferase / Q000378:metabolism*; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D051379:Mice; D008811:Mice, Inbred DBA; D008862:Microsomes, Liver / Q000201:enzymology*; D011506:Proteins / Q000378:metabolism
D011506:Proteins; D014453:Glucuronosyltransferase